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1uw8

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[[Image:1uw8.gif|left|200px]]
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[[Image:1uw8.png|left|200px]]
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{{STRUCTURE_1uw8| PDB=1uw8 | SCENE= }}
{{STRUCTURE_1uw8| PDB=1uw8 | SCENE= }}
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'''CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE'''
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===CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE===
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==Overview==
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Oxalate decarboxylase (EC 4.1.1.2) catalyzes the conversion of oxalate to formate and carbon dioxide and utilizes dioxygen as a cofactor. By contrast, the evolutionarily related oxalate oxidase (EC 1.2.3.4) converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. Divergent free radical catalytic mechanisms have been proposed for these enzymes that involve the requirement of an active site proton donor in the decarboxylase but not the oxidase reaction. The oxidase possesses only one domain and manganese binding site per subunit, while the decarboxylase has two domains and two manganese sites per subunit. A structure of the decarboxylase together with a limited mutagenesis study has recently been interpreted as evidence that the C-terminal domain manganese binding site (site 2) is the catalytic site and that Glu-333 is the crucial proton donor (Anand, R., Dorrestein, P. C., Kinsland, C., Begley, T. P., and Ealick, S. E. (2002) Biochemistry 41, 7659-7669). The N-terminal binding site (site 1) of this structure is solvent-exposed (open) and lacks a suitable proton donor for the decarboxylase reaction. We report a new structure of the decarboxylase that shows a loop containing a 3(10) helix near site 1 in an alternative conformation. This loop adopts a "closed" conformation forming a lid covering the entrance to site 1. This conformational change brings Glu-162 close to the manganese ion, making it a new candidate for the crucial proton donor. Site-directed mutagenesis of equivalent residues in each domain provides evidence that Glu-162 performs this vital role and that the N-terminal domain is either the sole or the dominant catalytically active domain.
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(as it appears on PubMed at http://www.pubmed.gov), where 14871895 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14871895}}
==About this Structure==
==About this Structure==
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[[Category: Metal binding protein]]
[[Category: Metal binding protein]]
[[Category: Oxalate]]
[[Category: Oxalate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:45:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:55:59 2008''

Revision as of 02:56, 29 July 2008

Image:1uw8.png

Template:STRUCTURE 1uw8

CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE

Template:ABSTRACT PUBMED 14871895

About this Structure

1UW8 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

A closed conformation of Bacillus subtilis oxalate decarboxylase OxdC provides evidence for the true identity of the active site., Just VJ, Stevenson CE, Bowater L, Tanner A, Lawson DM, Bornemann S, J Biol Chem. 2004 May 7;279(19):19867-74. Epub 2004 Feb 10. PMID:14871895

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